|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
17-594 |
3.55e-140 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 419.54 E-value: 3.55e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 17 DRGTLQVLQDMASRLRIHSIRATCSTSSGHPTSCSSSSEIMSVLFFYIMRYKQSDPENPDNDRFVLAK------------ 84
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAghgsmllysllh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 85 ----------------------------RLSFVDVATGWLGQGLGVACGMAYTGKY----FDRAS-----YRVFCLMSDG 127
Cdd:PRK05899 81 lagydlsiddlknfrqlgsktpghpeygHTPGVETTTGPLGQGLANAVGMALAEKYlaalFNRPGldivdHYTYVLCGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 128 ESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPaEHCINIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKh 207
Cdd:PRK05899 161 DLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTE-GWFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKAST- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 208 KPTAVVAKTFKGRGTPSIEDAESWHAKPMPRERADAIIKLIesqiqtsrNLDPqppiedspevnitdvrmtsppdyrvgd 287
Cdd:PRK05899 239 KPTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKEL--------GWDY--------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 288 kiatRKACGLALAKLGYANNRVVVLDGD------TRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRTIAFAS 361
Cdd:PRK05899 284 ----RKASGKALNALAKALPELVGGSADlagsnnTKIKGSKDFAPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 362 TFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAK-G 440
Cdd:PRK05899 360 TFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALERKdG 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 441 MCFIRTTRPETMVIY-TPQERFEIGQAKVLRHCvsDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVAti 519
Cdd:PRK05899 440 PSALVLTRQNLPVLErTAQEEGVAKGGYVLRDD--PDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ-- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 520 vssakategriitvEDHYPQGGIGEAVCAAVSMDPDI----------QVHSLAVSGVPQSGKSEELLDMYGISARHIIVA 589
Cdd:PRK05899 516 --------------DAAYKESVLPAAVTARVAVEAGVadgwykyvglDGKVLGIDTFGASAPADELFKEFGFTVENIVAA 581
|
....*
gi 158257954 590 VKCML 594
Cdd:PRK05899 582 AKELL 586
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
287-591 |
1.06e-110 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 333.59 E-value: 1.06e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 287 DKIATRKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRtIAFASTFAAF 366
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 367 LT-RAFDHIRI-GGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFI 444
Cdd:COG3958 81 LTgRAYEQIRNdIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 445 RTTRPETMVIYTPQERFEIGQAKVLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAK 524
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLRE--GKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158257954 525 ATeGRIITVEDHYPQGGIGEAVCAAVSMDPDIQVHSLAVSGVP-QSGKSEELLDMYGISARHIIVAVK 591
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFgESGSPEELLEKYGLDAEGIVAAAK 305
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
30-245 |
2.90e-84 |
|
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.
Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 263.60 E-value: 2.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 30 RLRIHSIRATCSTSSGHPTSCSSSSEIMSVLFFYIMRYKQSDPENPDNDRFVLAK------------------------- 84
Cdd:cd02012 2 RIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKghaspalyavlalagylpeedlktf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 85 -----RL---------SFVDVATGWLGQGLGVACGMAYTGKYFdRASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLV 150
Cdd:cd02012 82 rqlgsRLpghpeygltPGVEVTTGSLGQGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 151 AIFDVNRLGHSGALPAEHCINIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAES 230
Cdd:cd02012 161 AIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTAK 240
|
250
....*....|....*
gi 158257954 231 WHAKPMPRERADAII 245
Cdd:cd02012 241 WHGKPLGEEEVELAK 255
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
287-453 |
2.36e-46 |
|
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.
Pssm-ID: 460692 [Multi-domain] Cd Length: 174 Bit Score: 160.79 E-value: 2.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 287 DKIATRKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPE---RFIECFMAEQNMVSVALGCASRGR-TIAFAST 362
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 363 FAAFLTRAFDHIRIG-GLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAV--ALAANAK 439
Cdd:pfam02779 81 FSDFLNRADDAIRHGaALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLraAIRRDGR 160
|
170
....*....|....
gi 158257954 440 GMCFIRTTRPETMV 453
Cdd:pfam02779 161 KPVVLRLPRQLLRP 174
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
26-515 |
4.40e-46 |
|
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial transketolases. The group includes two from the yeast Saccharomyces cerevisiae but excludes dihydroxyactetone synthases (formaldehyde transketolases) from various yeasts and the even more distant mammalian transketolases. Among the family of thiamine diphosphate-dependent enzymes that includes transketolases, dihydroxyacetone synthases, pyruvate dehydrogenase E1-beta subunits, and deoxyxylulose-5-phosphate synthases, mammalian and bacterial transketolases seem not to be orthologous. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 272974 [Multi-domain] Cd Length: 653 Bit Score: 172.59 E-value: 4.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 26 DMASRLRIHSIRATCSTSSGHPTSCSSSSEIMSVLFFYIMRYkqsDPENP---DNDRFVLA------------------- 83
Cdd:TIGR00232 2 KLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKF---NPTNPkwiNRDRFVLSnghgsmllysllhltgydl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 84 -----KR----------------LSFVDVATGWLGQGLGVACGMAYTGKY----FDRASYRVF-----CLMSDGESSEGS 133
Cdd:TIGR00232 79 siedlKQfrqlhsktpghpeyghTAGVEATTGPLGQGIANAVGMAIAEKTlaatFNKPGFEIVdhytyVFVGDGCLQEGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 134 VWEAMAFASYYSLDNLVAIFDVNRLGHSGALPAEHCINIyQRRCEAFGWNT-YVVDGRDVEALCQVFWQASQVKHKPTAV 212
Cdd:TIGR00232 159 SYEVASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDV-AKRFEAYGWEVlEVEDGHDLAAIDAAIEEAKASTDKPTLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 213 VAKTFKGRGTPSIEDAESWHAKPMprerADAIIKLIESQIQTSRN----------------LDPQPPIEDS--------- 267
Cdd:TIGR00232 238 EVKTTIGFGSPNKAGTHGVHGAPL----GDEEVALTKKNLGWNYNpfeipqevydhfkktvKERGAKAEQEwnelfaayk 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 268 ---PEVNITDVRMTSP----------PDYRVGDK-IATRKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFN----KEY 329
Cdd:TIGR00232 314 kkyPELAAEFTRRLSGelpadwdkqlPEFKVKLQaLATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGsgdlHEN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 330 P-ERFIECFMAEQNMVSVALGCASRGRTIAFASTFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDGASQMALEDI 408
Cdd:TIGR00232 394 PlGNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 409 AMFRTIPKCTIFYPTDAVSTEHAVALAanakgmcfIRTTRPETMVIYTPQ----------ERFEIGqAKVLRHCVSDKVT 478
Cdd:TIGR00232 474 ASLRAIPNLSVWRPCDGNETAAAWKYA--------LESQDGPTALILSRQnlpqleesslEKVLKG-GYVLKDSKGPDLI 544
|
570 580 590
....*....|....*....|....*....|....*..
gi 158257954 479 VIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLD 515
Cdd:TIGR00232 545 LIATGSEVQLAVEAAKKLAAENIKVRVVSMPSFDLFD 581
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
320-448 |
2.06e-28 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 110.27 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 320 TFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRtIAFASTFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDG 399
Cdd:smart00861 4 ATRKAFGEALAELAIDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDG 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 158257954 400 ASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFIRTTR 448
Cdd:smart00861 83 PTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLER 131
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
17-594 |
3.55e-140 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 419.54 E-value: 3.55e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 17 DRGTLQVLQDMASRLRIHSIRATCSTSSGHPTSCSSSSEIMSVLFFYIMRYKQSDPENPDNDRFVLAK------------ 84
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAghgsmllysllh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 85 ----------------------------RLSFVDVATGWLGQGLGVACGMAYTGKY----FDRAS-----YRVFCLMSDG 127
Cdd:PRK05899 81 lagydlsiddlknfrqlgsktpghpeygHTPGVETTTGPLGQGLANAVGMALAEKYlaalFNRPGldivdHYTYVLCGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 128 ESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPaEHCINIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKh 207
Cdd:PRK05899 161 DLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTE-GWFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKAST- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 208 KPTAVVAKTFKGRGTPSIEDAESWHAKPMPRERADAIIKLIesqiqtsrNLDPqppiedspevnitdvrmtsppdyrvgd 287
Cdd:PRK05899 239 KPTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKEL--------GWDY--------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 288 kiatRKACGLALAKLGYANNRVVVLDGD------TRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRTIAFAS 361
Cdd:PRK05899 284 ----RKASGKALNALAKALPELVGGSADlagsnnTKIKGSKDFAPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 362 TFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAK-G 440
Cdd:PRK05899 360 TFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALERKdG 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 441 MCFIRTTRPETMVIY-TPQERFEIGQAKVLRHCvsDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVAti 519
Cdd:PRK05899 440 PSALVLTRQNLPVLErTAQEEGVAKGGYVLRDD--PDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ-- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 520 vssakategriitvEDHYPQGGIGEAVCAAVSMDPDI----------QVHSLAVSGVPQSGKSEELLDMYGISARHIIVA 589
Cdd:PRK05899 516 --------------DAAYKESVLPAAVTARVAVEAGVadgwykyvglDGKVLGIDTFGASAPADELFKEFGFTVENIVAA 581
|
....*
gi 158257954 590 VKCML 594
Cdd:PRK05899 582 AKELL 586
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
287-591 |
1.06e-110 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 333.59 E-value: 1.06e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 287 DKIATRKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRtIAFASTFAAF 366
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 367 LT-RAFDHIRI-GGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFI 444
Cdd:COG3958 81 LTgRAYEQIRNdIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 445 RTTRPETMVIYTPQERFEIGQAKVLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAK 524
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLRE--GKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158257954 525 ATeGRIITVEDHYPQGGIGEAVCAAVSMDPDIQVHSLAVSGVP-QSGKSEELLDMYGISARHIIVAVK 591
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFgESGSPEELLEKYGLDAEGIVAAAK 305
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
30-245 |
2.90e-84 |
|
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.
Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 263.60 E-value: 2.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 30 RLRIHSIRATCSTSSGHPTSCSSSSEIMSVLFFYIMRYKQSDPENPDNDRFVLAK------------------------- 84
Cdd:cd02012 2 RIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKghaspalyavlalagylpeedlktf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 85 -----RL---------SFVDVATGWLGQGLGVACGMAYTGKYFdRASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLV 150
Cdd:cd02012 82 rqlgsRLpghpeygltPGVEVTTGSLGQGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 151 AIFDVNRLGHSGALPAEHCINIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAES 230
Cdd:cd02012 161 AIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTAK 240
|
250
....*....|....*
gi 158257954 231 WHAKPMPRERADAII 245
Cdd:cd02012 241 WHGKPLGEEEVELAK 255
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
17-253 |
1.66e-67 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 220.72 E-value: 1.66e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 17 DRGTLQVLQDMASRLRIHSIRATCSTSSGHPTSCSSSSEIMSVLFFYIMRYKQSDPENPDNDRFVLAK------------ 84
Cdd:COG3959 1 TKEDIKELEEKARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKghaapalyavla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 85 RLSF---------------------------VDVATGWLGQGLGVACGMAYTGKYfDRASYRVFCLMSDGESSEGSVWEA 137
Cdd:COG3959 81 EKGYfpkeelatfrklgsrlqghpdmkktpgVEMSTGSLGQGLSVAVGMALAAKL-DGKDYRVYVLLGDGELQEGQVWEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 138 MAFASYYSLDNLVAIFDVNRLGHSGalPAEHCINIY--QRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKHKPTAVVAK 215
Cdd:COG3959 160 AMAAAHYKLDNLIAIVDRNGLQIDG--PTEDVMSLEplAEKWEAFGWHVIEVDGHDIEALLAALDEAKAVKGKPTVIIAH 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 158257954 216 TFKGRGTPSIEDAESWHAKPMPRERADAIIKLIESQIQ 253
Cdd:COG3959 238 TVKGKGVSFMENRPKWHGKAPNDEELEQALAELEAELG 275
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
293-448 |
2.85e-59 |
|
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and the beta subunits of the E1 component of the human pyruvate dehydrogenase complex (E1- PDHc), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Like many TPP-dependent enzymes DXS and TK are homodimers having a PYR and a PP domain on the same subunit. TK has two active sites per dimer which lie between PYR and PP domains of different subunits. For DXS each active site is located at the interface of a PYR and a PP domain from the same subunit. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites but having the PYR and PP domains arranged on separate subunits, the PYR domains on the beta subunits, the PP domains on the alpha subunits. DXS is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis, it catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. TK also plays a central role in the Calvin cycle in plants. PDHc catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. This subfamily includes the beta subunits of the E1 component of the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). ADC participates in the breakdown of acetoin. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids.
Pssm-ID: 132916 [Multi-domain] Cd Length: 156 Bit Score: 194.58 E-value: 2.85e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 293 KACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGrTIAFASTFAAFLTRAFD 372
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQRAYD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158257954 373 HIRI-GGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFIRTTR 448
Cdd:cd07033 80 QIRHdVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
287-453 |
2.36e-46 |
|
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.
Pssm-ID: 460692 [Multi-domain] Cd Length: 174 Bit Score: 160.79 E-value: 2.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 287 DKIATRKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPE---RFIECFMAEQNMVSVALGCASRGR-TIAFAST 362
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 363 FAAFLTRAFDHIRIG-GLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAV--ALAANAK 439
Cdd:pfam02779 81 FSDFLNRADDAIRHGaALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLraAIRRDGR 160
|
170
....*....|....
gi 158257954 440 GMCFIRTTRPETMV 453
Cdd:pfam02779 161 KPVVLRLPRQLLRP 174
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
26-515 |
4.40e-46 |
|
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial transketolases. The group includes two from the yeast Saccharomyces cerevisiae but excludes dihydroxyactetone synthases (formaldehyde transketolases) from various yeasts and the even more distant mammalian transketolases. Among the family of thiamine diphosphate-dependent enzymes that includes transketolases, dihydroxyacetone synthases, pyruvate dehydrogenase E1-beta subunits, and deoxyxylulose-5-phosphate synthases, mammalian and bacterial transketolases seem not to be orthologous. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 272974 [Multi-domain] Cd Length: 653 Bit Score: 172.59 E-value: 4.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 26 DMASRLRIHSIRATCSTSSGHPTSCSSSSEIMSVLFFYIMRYkqsDPENP---DNDRFVLA------------------- 83
Cdd:TIGR00232 2 KLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKF---NPTNPkwiNRDRFVLSnghgsmllysllhltgydl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 84 -----KR----------------LSFVDVATGWLGQGLGVACGMAYTGKY----FDRASYRVF-----CLMSDGESSEGS 133
Cdd:TIGR00232 79 siedlKQfrqlhsktpghpeyghTAGVEATTGPLGQGIANAVGMAIAEKTlaatFNKPGFEIVdhytyVFVGDGCLQEGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 134 VWEAMAFASYYSLDNLVAIFDVNRLGHSGALPAEHCINIyQRRCEAFGWNT-YVVDGRDVEALCQVFWQASQVKHKPTAV 212
Cdd:TIGR00232 159 SYEVASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDV-AKRFEAYGWEVlEVEDGHDLAAIDAAIEEAKASTDKPTLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 213 VAKTFKGRGTPSIEDAESWHAKPMprerADAIIKLIESQIQTSRN----------------LDPQPPIEDS--------- 267
Cdd:TIGR00232 238 EVKTTIGFGSPNKAGTHGVHGAPL----GDEEVALTKKNLGWNYNpfeipqevydhfkktvKERGAKAEQEwnelfaayk 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 268 ---PEVNITDVRMTSP----------PDYRVGDK-IATRKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFN----KEY 329
Cdd:TIGR00232 314 kkyPELAAEFTRRLSGelpadwdkqlPEFKVKLQaLATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGsgdlHEN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 330 P-ERFIECFMAEQNMVSVALGCASRGRTIAFASTFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDGASQMALEDI 408
Cdd:TIGR00232 394 PlGNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 409 AMFRTIPKCTIFYPTDAVSTEHAVALAanakgmcfIRTTRPETMVIYTPQ----------ERFEIGqAKVLRHCVSDKVT 478
Cdd:TIGR00232 474 ASLRAIPNLSVWRPCDGNETAAAWKYA--------LESQDGPTALILSRQnlpqleesslEKVLKG-GYVLKDSKGPDLI 544
|
570 580 590
....*....|....*....|....*....|....*..
gi 158257954 479 VIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLD 515
Cdd:TIGR00232 545 LIATGSEVQLAVEAAKKLAAENIKVRVVSMPSFDLFD 581
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
178-594 |
2.96e-42 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 160.25 E-value: 2.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 178 EAFGWNtYV--VDGRDVEALCQVFWQASQVKHkPTAVVAKTFKGRG-TPSIEDAESWHAkpmpreradaiikliesqiqt 254
Cdd:PRK05444 203 EELGFN-YIgpIDGHDLDALIETLKNAKDLKG-PVLLHVVTKKGKGyAPAEADPIKYHG--------------------- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 255 srnldpqppiedspevnitdvrmTSPPDYRVGDKIATRKAC--------GLALAKLGYANNRVVVLDGDTRYSTFSEIFN 326
Cdd:PRK05444 260 -----------------------VGKFDPETGEQPKSSKPGkpsytkvfGETLCELAEKDPKIVAITAAMPEGTGLVKFS 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 327 KEYPERFIECFMAEQNMVSVALGCASRGrTIAFASTFAAFLTRAFDHI----------------RiGGLaesniniigsh 390
Cdd:PRK05444 317 KRFPDRYFDVGIAEQHAVTFAAGLATEG-LKPVVAIYSTFLQRAYDQVihdvalqnlpvtfaidR-AGL----------- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 391 cgvsVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANA-KGMCFIRTTRPE-TMVIYTPQERFEIGQAKV 468
Cdd:PRK05444 384 ----VGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYdDGPIAIRYPRGNgVGVELPELEPLPIGKGEV 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 469 LRHcvSDKVTVIGAGITVYEALAAADELSKqdifIRVIDLFTIKPLDVATIVSSAKATEgRIITVEDHYPQGGIGEAVCA 548
Cdd:PRK05444 460 LRE--GEDVAILAFGTMLAEALKAAERLAS----ATVVDARFVKPLDEELLLELAAKHD-LVVTVEEGAIMGGFGSAVLE 532
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 158257954 549 AVS-MDPDIQVHSLavsGVPQS----GKSEELLDMYGISARHIIVAVKCML 594
Cdd:PRK05444 533 FLAdHGLDVPVLNL---GLPDEfidhGSREELLAELGLDAEGIARRILELL 580
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
178-594 |
8.62e-42 |
|
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and metabolism]; Deoxyxylulose-5-phosphate synthase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 440768 [Multi-domain] Cd Length: 623 Bit Score: 159.79 E-value: 8.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 178 EAFGWNtYV--VDGRDVEALCQVFWQASQVKhKPTAVVAKTFKGRG-TPSIEDAESWHAkpmpreradaiikliesqiqt 254
Cdd:COG1154 242 EELGFK-YIgpIDGHDLDALVETLRNAKDLK-GPVLLHVVTKKGKGyAPAEKDPDKFHG--------------------- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 255 srnldpQPPIEdsPEVNITDVRMTSPPDYrvgdkiaTrKACGLALAKLGYANNRVVV-----LDGdtrysTFSEIFNKEY 329
Cdd:COG1154 299 ------VGPFD--PETGEPKKSKSSAPSY-------T-DVFGDTLVELAEKDPRIVAitaamPEG-----TGLDKFAERF 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 330 PERFIECFMAEQNMVSVALGCASRGRTIAFA--STFaafLTRAFDHI----------------RiGGLaesniniigshc 391
Cdd:COG1154 358 PDRFFDVGIAEQHAVTFAAGLATEGLKPVVAiySTF---LQRAYDQVihdvalqnlpvtfaidR-AGL------------ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 392 gvsVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFIRTTR-PETMV-IYTPQERFEIGQAKVL 469
Cdd:COG1154 422 ---VGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRgNGPGVeLPAELEPLPIGKGEVL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 470 RHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATEgRIITVEDHYPQGGIGEAVCAA 549
Cdd:COG1154 499 RE--GKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHD-LVVTVEEGVLAGGFGSAVLEF 575
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 158257954 550 VS-MDPDIQVHSLavsGVPQS----GKSEELLDMYGISARHIIVAVKCML 594
Cdd:COG1154 576 LAdAGLDVPVLRL---GLPDRfiehGSRAELLAELGLDAEGIARAILELL 622
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
43-594 |
8.54e-37 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 145.59 E-value: 8.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 43 SSGHPTSCSSSSEIMSVLFFYIMRYKQSDPENPDNDRFVL----AKRLSF------------------------------ 88
Cdd:PTZ00089 25 NSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLsnghASALLYsmlhltgydlsmedlknfrqlgsrtpghpe 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 89 ------VDVATGWLGQGLGVACGMAYTGKY----FDRASY-----RVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIF 153
Cdd:PTZ00089 105 rhitpgVEVTTGPLGQGIANAVGLAIAEKHlaakFNRPGHpifdnYVYVICGDGCLQEGVSQEALSLAGHLGLEKLIVLY 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 154 DVNRLGHSGALPAEHCINIyQRRCEAFGWNTYVVD--GRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTpSIEDAESW 231
Cdd:PTZ00089 185 DDNKITIDGNTDLSFTEDV-EKKYEAYGWHVIEVDngNTDFDGLRKAIEEAKKSKGKPKLIIVKTTIGYGS-SKAGTEKV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 232 HAKPMPRERADAIIKLIesqiqtsrNLDPQPPIEDSPEV--------------------NITDVRMTSP----------- 280
Cdd:PTZ00089 263 HGAPLGDEDIAQVKELF--------GLDPEKKFHVSEEVrqffeqhvekkkenyeawkkRFAKYTAAFPkeaqaierrfk 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 281 -----------PDYRVGDK-IATRKACGLALAKLGYANNRVVVLDGD------TRYSTFSEIFNKEYPERFIECFMAEQN 342
Cdd:PTZ00089 335 gelppgwekklPKYTTNDKaIATRKASENVLNPLFQILPELIGGSADltpsnlTRPKEANDFTKASPEGRYIRFGVREHA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 343 MVSVALGCASRGRTIAFASTFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYP 422
Cdd:PTZ00089 415 MCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALLRATPNLLVIRP 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 423 TDAVSTEHAVALA-ANAKGMCFIRTTRPETMVIYTPQERFEIGQAKVLRHC-VSDKVTVIGAGITVYEALAAADELSKqD 500
Cdd:PTZ00089 495 ADGTETSGAYALAlANAKTPTILCLSRQNTPPLPGSSIEGVLKGAYIVVDFtNSPQLILVASGSEVSLCVEAAKALSK-E 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 501 IFIRVI-----DLFTIKPLDVATIVssakategriitvedhYPQGGIGE-AVCAAVSMDPDIQVH-SLAVSGVPQSGKSE 573
Cdd:PTZ00089 574 LNVRVVsmpcwELFDQQSEEYQQSV----------------LPSGGVPVlSVEAYVSFGWEKYSHvHVGISGFGASAPAN 637
|
650 660
....*....|....*....|.
gi 158257954 574 ELLDMYGISARHIIVAVKCML 594
Cdd:PTZ00089 638 ALYKHFGFTVENVVEKARALA 658
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
464-586 |
8.38e-36 |
|
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site.
Pssm-ID: 460693 [Multi-domain] Cd Length: 124 Bit Score: 130.41 E-value: 8.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 464 GQAKVLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATeGRIITVEDHYPQGGIG 543
Cdd:pfam02780 1 GKAEILRE--GDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKT-GRLVTVEEAVPRGGFG 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 158257954 544 EAVCAAVS----MDPDIQVHSLAVSGVPQSGKSEELLDMYGISARHI 586
Cdd:pfam02780 78 SEVAAALAeeafDGLDAPVLRVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| PLN02790 |
PLN02790 |
transketolase |
32-508 |
2.09e-31 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 129.37 E-value: 2.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 32 RIHSIRATCSTSSGHPTSCSSSSEIMSVLFFYIMRYKQSDPENPDNDRFVLA-------------------------KRL 86
Cdd:PLN02790 2 RFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSaghgcmlqyallhlagydsvqmedlKQF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 87 ------------SF----VDVATGWLGQGLGVACGMAYTGKY----FDRA-----SYRVFCLMSDGESSEGSVWEAMAFA 141
Cdd:PLN02790 82 rqwgsrtpghpeNFetpgIEVTTGPLGQGIANAVGLALAEKHlaarFNKPdhkivDHYTYCILGDGCQMEGISNEAASLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 142 SYYSLDNLVAIFDVNRL---GHSGALPAEHCIniyqRRCEAFGWNTYVVDG--RDVEALCQVFWQASQVKHKPTAVVAKT 216
Cdd:PLN02790 162 GHWGLGKLIVLYDDNHIsidGDTEIAFTEDVD----KRYEALGWHTIWVKNgnTDYDEIRAAIKEAKAVTDKPTLIKVTT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 217 FKGRGTPSIEDAESWHAKPMPRERADAiikliesqiqTSRNLD-PQPPIEDSPEVN------------------------ 271
Cdd:PLN02790 238 TIGYGSPNKANSYSVHGAALGEKEVDA----------TRKNLGwPYEPFHVPEDVKshwskhtkegaaleaewnakfaey 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 272 --------------ITDVRMT----SPPDYRVGDKI-ATRK---ACGLALAKL------GYAN----NRVVVLD-GDtry 318
Cdd:PLN02790 308 kkkypeeaaelkslISGELPSgwekALPTFTPEDPAdATRNlsqKCLNALAKVlpgligGSADlassNMTLLKDfGD--- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 319 stfseiFNKEYP-ERFIECFMAEQNMVSVALGCASRGRT-IAFASTFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVG 396
Cdd:PLN02790 385 ------FQKDTPeERNVRFGVREHGMGAICNGIALHSSGlIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 397 DDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALA-ANAKG---MCFIRTTRPETMViyTPQERFEIGQAKVLRHC 472
Cdd:PLN02790 459 EDGPTHQPIEHLASLRAMPNILMLRPADGNETAGAYKVAvTNRKRptvLALSRQKVPNLPG--TSIEGVEKGGYVISDNS 536
|
570 580 590
....*....|....*....|....*....|....*...
gi 158257954 473 VSDK--VTVIGAGITVYEALAAADELSKQDIFIRVIDL 508
Cdd:PLN02790 537 SGNKpdLILIGTGSELEIAAKAAKELRKEGKKVRVVSM 574
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
320-448 |
2.06e-28 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 110.27 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 320 TFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRtIAFASTFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDG 399
Cdd:smart00861 4 ATRKAFGEALAELAIDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDG 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 158257954 400 ASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFIRTTR 448
Cdd:smart00861 83 PTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLER 131
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
339-551 |
1.28e-25 |
|
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit [Energy production and conversion]; Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 439793 [Multi-domain] Cd Length: 325 Bit Score: 107.79 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 339 AEQNMVSVALGCASRG-RTIAFAsTFAAFLTRAFDHI---------RIGGLAESNInIIGSHCGVSVGDdGA--SQMaLE 406
Cdd:COG0022 59 SEAGIVGAAIGAALAGlRPVVEI-QFADFIYPAFDQIvnqaaklryMSGGQFKVPM-VIRTPYGGGIGA-GAqhSQS-LE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 407 diAMFRTIPKCTIFYPtdavSTehavalAANAKGM---CfIRTTRP----ETMVIYT-----PQERFE--IGQAKVLRHc 472
Cdd:COG0022 135 --AWFAHIPGLKVVAP----ST------PYDAKGLlkaA-IRDDDPviflEHKRLYRlkgevPEEDYTvpLGKARVVRE- 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158257954 473 vSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATeGRIITVEDHYPQGGIGEAVCAAVS 551
Cdd:COG0022 201 -GTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLSPLDEETILESVKKT-GRLVVVDEAPRTGGFGAEIAARIA 277
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
184-594 |
4.57e-25 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 109.81 E-value: 4.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 184 TYV--VDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAEswhakpmprERADAIIKLiesQIQTSRNLDPQ 261
Cdd:PRK12571 248 TYVgpIDGHDMEALLSVLRAARARADGPVLVHVVTEKGRGYAPAEADE---------DKYHAVGKF---DVVTGLQKKSA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 262 PpiedspevnitdvrmtSPPDYRvgdkiatrKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPERFIECFMAEQ 341
Cdd:PRK12571 316 P----------------SAPSYT--------SVFGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 342 NMVSVALGCASRGrTIAFASTFAAFLTRAFDHIRIG-GLAESNINIIGSHCGVsVGDDGASQMALEDIAMFRTIPKCTIF 420
Cdd:PRK12571 372 HAVTFAAGLAAAG-LKPFCAVYSTFLQRGYDQLLHDvALQNLPVRFVLDRAGL-VGADGATHAGAFDLAFLTNLPNMTVM 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 421 YPTDAVSTEHAVALA-ANAKGMCFIRTTRPETMVIYTPqERFEIGQAKVLRHCVSDK-VTVIGAGITVYEALAAADELSK 498
Cdd:PRK12571 450 APRDEAELRHMLRTAaAHDDGPIAVRFPRGEGVGVEIP-AEGTILGIGKGRVPREGPdVAILSVGAHLHECLDAADLLEA 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 499 QDIFIRVIDLFTIKPLDVATIvssAKATEGRI-ITVEDHYPQGGIGEAVCAAVS----MDPDIQVHSLavsGVP----QS 569
Cdd:PRK12571 529 EGISVTVADPRFVKPLDEALT---DLLVRHHIvVIVEEQGAMGGFGAHVLHHLAdtglLDGGLKLRTL---GLPdrfiDH 602
|
410 420
....*....|....*....|....*
gi 158257954 570 GKSEELLDMYGISARHIIVAVKCML 594
Cdd:PRK12571 603 ASREEMYAEAGLTAPDIAAAVTGAL 627
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
25-270 |
5.36e-24 |
|
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.
Pssm-ID: 395366 [Multi-domain] Cd Length: 334 Bit Score: 103.24 E-value: 5.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 25 QDMASRLRIHSIRATCSTSSGHPTSCSSSSEIMSVLFFYIMRYKQSDPENPDNDRFVL---------------------- 82
Cdd:pfam00456 3 KRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLsnghgsmllysllhltgydlsm 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 83 AKRLSF------------------VDVATGWLGQGLGVACGMA---------YTGKYFDRASYRVFCLMSDGESSEGSVW 135
Cdd:pfam00456 83 EDLKSFrqlgsktpghpefghtagVEVTTGPLGQGIANAVGMAiaernlaatYNRPGFDIVDHYTYVFLGDGCLMEGVSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 136 EAMAFASYYSLDNLVAIFDVNRLGHSGALPAEHCINIyQRRCEAFGWNT-YVVDGRDVEALCQVFWQASQVKHKPTAVVA 214
Cdd:pfam00456 163 EASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDT-AARFEAYGWHViEVEDGHDVEAIAAAIEEAKAEKDKPTLIKC 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 158257954 215 KTFKGRGTPSIEDAESWHAKPMpreRADAIiklieSQIQTSRNLDPQPPIEDSPEV 270
Cdd:pfam00456 242 RTVIGYGSPNKQGTHDVHGAPL---GADEV-----AALKQKLGWDPYKPFEIPAEV 289
|
|
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
44-509 |
7.92e-23 |
|
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439792 [Multi-domain] Cd Length: 661 Bit Score: 102.78 E-value: 7.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 44 SGHPTSCSSSSEIMSVLFFYIMRYkqsDPENP---DNDRFVLA------------------------KRL---------- 86
Cdd:COG0021 24 SGHPGLPMGMAPIAYVLWTKFLKH---NPANPkwpNRDRFVLSaghgsmllysllhltgydlslddlKNFrqlgsktpgh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 87 ------SFVDVATGWLGQGLGVACGMAYTGKY----FDRASY-----RVFCLMSDGESSEGSVWEAMAFASYYSLDNLVA 151
Cdd:COG0021 101 peyghtPGVETTTGPLGQGIANAVGMAIAERHlaarFNRPGHdivdhYTYVIAGDGDLMEGISHEAASLAGHLKLGKLIV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 152 IFDVNRlghsgalpaehcINI-----------YQRRCEAFGWNTY-VVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKG 219
Cdd:COG0021 181 LYDDNG------------ISIdgdtdlafsedVAKRFEAYGWHVIrVEDGHDLEAIDAAIEAAKAETDKPTLIICKTIIG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 220 RGTPSIEDAESWHAKPMPrerADAIIKLIEsqiqtsrNLD-PQPPIEDSPEV-NITD----------------------- 274
Cdd:COG0021 249 YGSPNKQGTAKAHGAPLG---AEEIAATKE-------ALGwPPEPFEVPDEVyAHWRaagergaaaeaewnerfaayaaa 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 275 --------VRMTSP----------PDYRVGDK-IATRKACGLALAKLGYANNRVVV----LDGdtrySTFSEI-----FN 326
Cdd:COG0021 319 ypelaaelERRLAGelpedwdaalPAFEADAKgVATRKASGKVLNALAPVLPELIGgsadLAG----SNKTTIkgagsFS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 327 KEYPE-RFIECFMAEQNMVSVALGCASRGRTIAFASTFAAFltraFDH----IRIGGLAESNINIIGSHCGVSVGDDGAS 401
Cdd:COG0021 395 PEDPSgRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVF----SDYmrpaIRLAALMKLPVIYVFTHDSIGLGEDGPT 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 402 QMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANakgmcfiRTTRPeTMVIYT----PQERFEIGQAK-------VLR 470
Cdd:COG0021 471 HQPVEQLASLRAIPNLDVIRPADANETAAAWKLALE-------RKDGP-TALILSrqnlPTLDRTAAAAEgvakgayVLA 542
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 158257954 471 HCVSD-KVTVIGAGITVYEALAAADELSKQDIFIRVI-----DLF 509
Cdd:COG0021 543 DAEGTpDVILIATGSEVSLAVEAAELLAAEGIKVRVVsmpswELF 587
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
330-550 |
1.50e-21 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 96.59 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 330 PERFIECFMAEQNMVSVALGCASRG-RTIAfASTFAAFLTRAFDHI---------RIGGLAESNInIIGSHCGVsVGDDG 399
Cdd:PTZ00182 81 PDRVFDTPITEQGFAGFAIGAAMNGlRPIA-EFMFADFIFPAFDQIvneaakyryMSGGQFDCPI-VIRGPNGA-VGHGG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 400 A--SQmALEdiAMFRTIPKCTIFYPTDAVstehavalaaNAKGMCF--IRTTRP----ETMVIY------TPQERFE--I 463
Cdd:PTZ00182 158 AyhSQ-SFE--AYFAHVPGLKVVAPSDPE----------DAKGLLKaaIRDPNPvvffEPKLLYresvevVPEADYTlpL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 464 GQAKVLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATeGRIITVEDHYPQGGIG 543
Cdd:PTZ00182 225 GKAKVVRE--GKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKT-GRCVIVHEAPPTCGIG 301
|
....*..
gi 158257954 544 EAVCAAV 550
Cdd:PTZ00182 302 AEIAAQI 308
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
96-553 |
5.20e-19 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 90.93 E-value: 5.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 96 LGQGLGVACGMAYTGkyfdrASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFD--------VNRLGHSGALPAE 167
Cdd:PLN02234 183 LSAGLGMAVGRDLKG-----MNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDnkqvslptANLDGPTQPVGAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 168 HC-INIYQRRC-----------EAFGWNtYV--VDGRDVEALCQVFWQASQVKH-KPTAVVAKTFKGRGTPSIEDAEswh 232
Cdd:PLN02234 258 SCaLSRLQSNCgmiretsstlfEELGFH-YVgpVDGHNIDDLVSILETLKSTKTiGPVLIHVVTEKGRGYPYAERAD--- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 233 akpmprERADAIIKLiesqiqtsrnlDPQppiedspevnitdvrmtSPPDYRVGDKIATRKACGL-ALAKLGYANNRVVV 311
Cdd:PLN02234 334 ------DKYHGVLKF-----------DPE-----------------TGKQFKNISKTQSYTSCFVeALIAEAEADKDIVA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 312 LDGDTRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRTiAFASTFAAFLTRAFDHI-RIGGLAESNINIIGSH 390
Cdd:PLN02234 380 IHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCTIYSSFMQRAYDQVvHDVDLQKLPVRFAIDR 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 391 CGVsVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAA--NAKGMCFiRTTRPETMVIYTPQER----FEIG 464
Cdd:PLN02234 459 AGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAaiDDRPSCF-RYHRGNGIGVSLPPGNkgvpLQIG 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 465 QAKVLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATEgRIITVEDHyPQGGIGE 544
Cdd:PLN02234 537 RGRILRD--GERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHE-VLITVEEG-SIGGFGS 612
|
....*....
gi 158257954 545 AVCAAVSMD 553
Cdd:PLN02234 613 HVVQFLALD 621
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
435-550 |
1.35e-18 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 88.82 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 435 AANAKGM--CFIRTTRPetmVIYTPQE-----RFE----------IGQAKVLRhcVSDKVTVIGAGITVYEALAAADELS 497
Cdd:PRK11892 289 AADAKGLlkAAIRDPNP---VIFLENEilygqSFDvpklddfvlpIGKARIHR--EGKDVTIVSFSIGMTYALKAAEELA 363
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 158257954 498 KQDIFIRVIDLFTIKPLDVATIVSSAKATeGRIITVEDHYPQGGIGEAVCAAV 550
Cdd:PRK11892 364 KEGIDAEVIDLRTIRPMDTETIVESVKKT-NRLVTVEEGWPQSGVGAEIAARV 415
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
330-550 |
1.01e-16 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 81.69 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 330 PERFIECFMAEQNMVSVALGCASRG-RTIAFASTFAaFLTRAFDHIrIGGLAESNInIIGSHCGVSV---GDDGA----- 400
Cdd:PRK09212 50 PKRVIDTPITEHGFAGLAVGAAFAGlRPIVEFMTFN-FSMQAIDQI-VNSAAKTNY-MSGGQLKCPIvfrGPNGAaarva 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 401 SQMALEDIAMFRTIPKCTIFYPtdavstehavALAANAKGM--CFIRTTRP----ETMVIY-----TPQERF--EIGQAK 467
Cdd:PRK09212 127 AQHSQCYAAWYSHIPGLKVVAP----------YFAADCKGLlkTAIRDPNPviflENEILYghsheVPEEEEsiPIGKAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 468 VLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATeGRIITVEDHYPQGGIGEAVC 547
Cdd:PRK09212 197 ILRE--GSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIIESVKKT-NRLVVVEEGWPFAGVGAEIA 273
|
...
gi 158257954 548 AAV 550
Cdd:PRK09212 274 ALI 276
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
324-553 |
5.34e-16 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 81.49 E-value: 5.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 324 IFNKEYPERFIECFMAEQNMVSVALGCASRGRTiAFASTFAAFLTRAFDHIRIG-GLAESNINIIGSHCGVsVGDDGASQ 402
Cdd:PLN02582 391 LFARRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCAIYSSFLQRGYDQVVHDvDLQKLPVRFAMDRAGL-VGADGPTH 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 403 MALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAA--NAKGMCFiRTTRPETMVIYTPQER----FEIGQAKVLRHcvSDK 476
Cdd:PLN02582 469 CGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAaiDDRPSCF-RYPRGNGIGVQLPPNNkgipIEVGKGRILLE--GER 545
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158257954 477 VTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATEgRIITVEDHyPQGGIGEAVCAAVSMD 553
Cdd:PLN02582 546 VALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKSHE-VLITVEEG-SIGGFGSHVAQFMALD 620
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
185-546 |
5.51e-16 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 81.21 E-value: 5.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 185 YVVDGRDVEALCQVFWQASQVKHkPTAVVAKTFKGRG-TPSIEDAESWHAKpMPReradaiikliesqiqtsrNLDPQPP 263
Cdd:PRK12315 212 YVEDGNDIESLIEAFKEVKDIDH-PIVLHIHTLKGKGyQPAEENKEAFHWH-MPF------------------DLETGQS 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 264 IEDSPEVNITDVRMtsppDYrVGDKIATRKacglalaklgyannRVVVLDGDTRySTFS-EIFNKEYPERFIECFMAEQN 342
Cdd:PRK12315 272 KVPASGESYSSVTL----DY-LLKKIKEGK--------------PVVAINAAIP-GVFGlKEFRKKYPDQYVDVGIAEQE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 343 MVSVALGCASRG-RTIAFasTFAAFLTRAFDHIrIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFY 421
Cdd:PRK12315 332 SVAFASGIAANGaRPVIF--VNSTFLQRAYDQL-SHDLAINNNPAVMIVFGGSISGNDVTHLGIFDIPMISNIPNLVYLA 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 422 PTDA-----------VSTEHAVAlaanakgmcfIRTtrPETMVIYTPQE-------RFEIGQAkvlrhcvSDKVTVIGAG 483
Cdd:PRK12315 409 PTTKeeliamlewalTQHEHPVA----------IRV--PEHGVESGPTVdtdystlKYEVTKA-------GEKVAILALG 469
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158257954 484 iTVYE-ALAAADELSKQD-IFIRVIDLFTIKPLDVATIvSSAKATEGRIITVEDHYPQGGIGEAV 546
Cdd:PRK12315 470 -DFYElGEKVAKKLKEELgIDATLINPKFITGLDEELL-EKLKEDHELVVTLEDGILDGGFGEKI 532
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
324-553 |
6.72e-15 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 76.40 E-value: 6.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 324 IFNKEYPERFIECFMAEQNMVSVALGCASRG-RTIAFASTFAaFLTRAFDHIrIGGLAESNINIIGShcgVSV-----GD 397
Cdd:PLN02683 67 LLQKYGPDRVLDTPITEAGFTGIGVGAAYAGlKPVVEFMTFN-FSMQAIDHI-INSAAKTNYMSAGQ---ISVpivfrGP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 398 DGAS-----QMALEDIAMFRTIPKCTIFYPTDAvstEHAVALAANAkgmcfIRTTRP----ETMVIY-----------TP 457
Cdd:PLN02683 142 NGAAagvgaQHSQCFAAWYSSVPGLKVLAPYSS---EDARGLLKAA-----IRDPDPvvflENELLYgesfpvsaevlDS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 458 QERFEIGQAKVLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATeGRIITVEDHY 537
Cdd:PLN02683 214 SFVLPIGKAKIERE--GKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKT-NRLVTVEEGW 290
|
250
....*....|....*.
gi 158257954 538 PQGGIGEAVCAAVSMD 553
Cdd:PLN02683 291 PQHGVGAEICASVVEE 306
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
325-594 |
4.33e-12 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 68.97 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 325 FNKEYPERFIECFMAEQNMVSVALGCASRGRTiAFASTFAAFLTRAFDH-IRIGGLAESNINIIGSHCGVsVGDDGASQM 403
Cdd:PLN02225 417 FQERFPDRFFNVGMAEQHAVTFSAGLSSGGLK-PFCIIPSAFLQRAYDQvVHDVDRQRKAVRFVITSAGL-VGSDGPVQC 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 404 ALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAA--NAKGMC--FIRTTRPETMVIYTPQERFEIGQAKVLRHcvSDKVTV 479
Cdd:PLN02225 495 GAFDIAFMSSLPNMIAMAPADEDELVNMVATAAyvTDRPVCfrFPRGSIVNMNYLVPTGLPIEIGRGRVLVE--GQDVAL 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 480 IGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVaTIVSSAKATEGRIITVEDHYpQGGIGEAVCAAVS----MDPD 555
Cdd:PLN02225 573 LGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDI-KLVRDLCQNHKFLITVEEGC-VGGFGSHVAQFIAldgqLDGN 650
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 158257954 556 IQVHSLAV-SGVPQSGKSEELLDMYGISARHIIVAVKCML 594
Cdd:PLN02225 651 IKWRPIVLpDGYIEEASPREQLALAGLTGHHIAATALSLL 690
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
92-217 |
3.52e-11 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 64.44 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 92 ATGWLGQGLGVACGMAYTGKYFDRASYrVFCLMSDGESSEGSVWEAMAFAsyySLDNLVAIFDV--NRLGHSGALP-AEH 168
Cdd:cd02000 102 GNGIVGGQVPLAAGAALALKYRGEDRV-AVCFFGDGATNEGDFHEALNFA---ALWKLPVIFVCenNGYAISTPTSrQTA 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 158257954 169 CINIYQrRCEAFGWNTYVVDGRDVEALCQVFWQASQ---VKHKPTAVVAKTF 217
Cdd:cd02000 178 GTSIAD-RAAAYGIPGIRVDGNDVLAVYEAAKEAVErarAGGGPTLIEAVTY 228
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
96-266 |
8.09e-11 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 63.62 E-value: 8.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 96 LGQGLGVACGMAYTGKYF--DRAsyrVFCLMSDGESSEGSVWEAMAFAsyySLDNLVAIFDV--NRLGHSGalPAEH--- 168
Cdd:COG1071 129 VGGQLPHAVGAALAAKLRgeDEV---AVAFFGDGATSEGDFHEALNFA---AVWKLPVVFVCenNGYAIST--PVERqta 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 169 CINIYQrRCEAFGWNTYVVDGRDVEALCQVFWQAsqVKH-----KPTAVVAKTFKGRG-----TPSI----EDAESWHAK 234
Cdd:COG1071 201 VETIAD-RAAGYGIPGVRVDGNDVLAVYAAVKEA--VERarageGPTLIEAKTYRLGGhstsdDPTRyrtkEEVEEWRER 277
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 158257954 235 -PMPR-------------ERADAIIKLIESQIQTSRNL---DPQPPIED 266
Cdd:COG1071 278 dPIERlraylleegllteEELEAIEAEAKAEVEEAVEFaeaSPEPDPEE 326
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
93-221 |
1.12e-06 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 49.47 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 93 TGWLGQGLGVACGMAytgKYFDRA--SYRVFCLMSDGESSEGSVWEAMAFASYYsLDNLVAIFDVNRlgHSGALPAEHCI 170
Cdd:cd02007 74 TGHSSTSISAALGMA---VARDLKgkKRKVIAVIGDGALTGGMAFEALNNAGYL-KSNMIVILNDNE--MSISPNVGTPG 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 158257954 171 NIYqrrcEAFGWN-TYVVDGRDVEALCQVFWQASQVKHkPTAVVAKTFKGRG 221
Cdd:cd02007 148 NLF----EELGFRyIGPVDGHNIEALIKVLKEVKDLKG-PVLLHVVTKKGKG 194
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
409-596 |
1.58e-06 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 50.51 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 409 AMFRTIPKCTIFyptdAVSTEHavalaaNAKGM--CFIRTTRP----ETMVIYT-----PQERF--EIGQAKVLRHcvSD 475
Cdd:CHL00144 135 SYFQSVPGLQIV----ACSTPY------NAKGLlkSAIRSNNPviffEHVLLYNlkeeiPDNEYllPLEKAEVVRP--GN 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 476 KVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATEgRIITVEDHYPQGGIGEAVCAAV----- 550
Cdd:CHL00144 203 DITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTISKSVKKTH-KVLIVEECMKTGGIGAELIAQInehlf 281
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 158257954 551 -SMDPDIQVHSLAVSGVPQSGKSEELLDmygISARHIIVAVKCMLLN 596
Cdd:CHL00144 282 dELDAPIVRLSSQDVPTPYNGPLEEATV---IQPAQIIEAVEQIITN 325
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
88-195 |
4.14e-06 |
|
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDC). PDC catalyzes the oxidative decarboxylation of pyruvate and the subsequent acetylation of coenzyme A to acetyl-CoA. The E1 component of PDC catalyzes the first step of the multistep process, using TPP and a divalent cation as cofactors. E. coli PDC is a homodimeric enzyme.
Pssm-ID: 238975 [Multi-domain] Cd Length: 386 Bit Score: 49.23 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 88 FVDVATGWLGQGLGVACGMAYTGKYFDRASY------RVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNR---- 157
Cdd:cd02017 112 FWEFPTVSMGLGPIQAIYQARFNRYLEDRGLkdtsdqKVWAFLGDGEMDEPESLGAIGLAAREKLDNLIFVVNCNLqrld 191
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 158257954 158 ---LGHSGAlpaehcINIYQRRCEAFGWN-TYVVDGRDVEAL 195
Cdd:cd02017 192 gpvRGNGKI------IQELEGIFRGAGWNvIKVIWGSKWDEL 227
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
80-216 |
3.05e-05 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 44.55 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 80 FVLAKRLSFVdVATGW--LGQGLGVACGMAYTGKyfDRasyRVFCLMSDGESSEGsvWEAMAFASYYSLDNLVAIFDVNR 157
Cdd:cd00568 31 LPLRRGRRFL-TSTGFgaMGYGLPAAIGAALAAP--DR---PVVCIAGDGGFMMT--GQELATAVRYGLPVIVVVFNNGG 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158257954 158 LG---------HSGALPAEHCINI-YQRRCEAFGWNTYVVDgrDVEALCQVFWQASQvKHKPTAVVAKT 216
Cdd:cd00568 103 YGtirmhqeafYGGRVSGTDLSNPdFAALAEAYGAKGVRVE--DPEDLEAALAEALA-AGGPALIEVKT 168
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
95-276 |
4.94e-05 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 45.63 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 95 WLGQGLGVACGMAYTGKYF-----DRASYRV-FCLMSDGESSEGSVWEAMAFASYYsldNLVAIFDVNR------LGH-- 160
Cdd:CHL00149 129 FIGEGIPIALGAAFQSIYRqqvlkEVQPLRVtACFFGDGTTNNGQFFECLNMAVLW---KLPIIFVVENnqwaigMAHhr 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158257954 161 SGALPAEHciniyqRRCEAFGWNTYVVDGRDVEALCQVFWQA---SQVKHKPTAVVAKTFKGRGTP--------SIEDAE 229
Cdd:CHL00149 206 STSIPEIH------KKAEAFGLPGIEVDGMDVLAVREVAKEAverARQGDGPTLIEALTYRFRGHSladpdelrSKQEKE 279
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158257954 230 SWHAKpmpreraDAIIKL----IESQIQTSRNLDP-----QPPIED-------SPEVNITDVR 276
Cdd:CHL00149 280 AWVAR-------DPIKKLksyiIDNELASQKELNKiqrevKIEIEQavqfaisSPEPNISDLK 335
|
|
| |
